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a6l  (Biorbyt)


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    Structured Review

    Biorbyt a6l
    Mitochondria isolated from cell lines were solubilised by digitonin 2 g/g protein, separated on clear-native PAGE (CNE) and either stained in gel for ATP hydrolytic activity or used for WB detection of F1-α, Fo-a, <t>A6L,</t> DAPIT and MLQ subunits. Individual forms of ATP synthase are indicated: cV M – monomer, cV D – dimer, cV o – oligomer, cV M * and cV D * denote smaller form of the respective complexes.
    A6l, supplied by Biorbyt, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/a6l/product/Biorbyt
    Average 91 stars, based on 1 article reviews
    a6l - by Bioz Stars, 2026-02
    91/100 stars

    Images

    1) Product Images from "MLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthase"

    Article Title: MLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthase

    Journal: bioRxiv

    doi: 10.1101/2020.02.03.931709

    Mitochondria isolated from cell lines were solubilised by digitonin 2 g/g protein, separated on clear-native PAGE (CNE) and either stained in gel for ATP hydrolytic activity or used for WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. Individual forms of ATP synthase are indicated: cV M – monomer, cV D – dimer, cV o – oligomer, cV M * and cV D * denote smaller form of the respective complexes.
    Figure Legend Snippet: Mitochondria isolated from cell lines were solubilised by digitonin 2 g/g protein, separated on clear-native PAGE (CNE) and either stained in gel for ATP hydrolytic activity or used for WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. Individual forms of ATP synthase are indicated: cV M – monomer, cV D – dimer, cV o – oligomer, cV M * and cV D * denote smaller form of the respective complexes.

    Techniques Used: Isolation, Clear Native PAGE, Staining, Activity Assay

    Mitochondria isolated from the respective cell lines were solubilised by digitonin 2 g/g and separated on blue-native PAGE (BNE). WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. ATP synthase forms: cV M – monomer, cV D – dimer, F 1 +c − F 1 and c subunits and F 1 subcomplexes.
    Figure Legend Snippet: Mitochondria isolated from the respective cell lines were solubilised by digitonin 2 g/g and separated on blue-native PAGE (BNE). WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. ATP synthase forms: cV M – monomer, cV D – dimer, F 1 +c − F 1 and c subunits and F 1 subcomplexes.

    Techniques Used: Isolation, Blue Native PAGE

    (A) MLQ KO and control cells were radioactively labelled for 3h with 35 S-methionin/cysteine and subsequently chased with cold methionine for 1, 2, and 3 days. Cells were harvested, solubilised with triton X-100 and ATP synthase was isolated by immune-affinity purification using ATP synthase immunocapture kit. IP-ATP synthase was than analysed by SDS-PAGE. Quantification of the radioactive signal of all ATP synthase subunits shows uniform kinetics of degradation in control HEK cells (B) , while (C) MLQ KO cells displayed faster turnover of subunits F o -a and A6L (red lines) but stabilization of the F 1 subunits (α and β, green lines) compared to subunits b, d and OSCP of the external stalk (blue line). Similar stabilisation of F 1 subunits show ΔTA cells ( E ) compared to control cybrids ( D ) as well as rho 0 cells ( G ) compared to control rho + cells ( F ).
    Figure Legend Snippet: (A) MLQ KO and control cells were radioactively labelled for 3h with 35 S-methionin/cysteine and subsequently chased with cold methionine for 1, 2, and 3 days. Cells were harvested, solubilised with triton X-100 and ATP synthase was isolated by immune-affinity purification using ATP synthase immunocapture kit. IP-ATP synthase was than analysed by SDS-PAGE. Quantification of the radioactive signal of all ATP synthase subunits shows uniform kinetics of degradation in control HEK cells (B) , while (C) MLQ KO cells displayed faster turnover of subunits F o -a and A6L (red lines) but stabilization of the F 1 subunits (α and β, green lines) compared to subunits b, d and OSCP of the external stalk (blue line). Similar stabilisation of F 1 subunits show ΔTA cells ( E ) compared to control cybrids ( D ) as well as rho 0 cells ( G ) compared to control rho + cells ( F ).

    Techniques Used: Control, Isolation, Affinity Purification, SDS Page



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    Image Search Results


    Mitochondria isolated from cell lines were solubilised by digitonin 2 g/g protein, separated on clear-native PAGE (CNE) and either stained in gel for ATP hydrolytic activity or used for WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. Individual forms of ATP synthase are indicated: cV M – monomer, cV D – dimer, cV o – oligomer, cV M * and cV D * denote smaller form of the respective complexes.

    Journal: bioRxiv

    Article Title: MLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthase

    doi: 10.1101/2020.02.03.931709

    Figure Lengend Snippet: Mitochondria isolated from cell lines were solubilised by digitonin 2 g/g protein, separated on clear-native PAGE (CNE) and either stained in gel for ATP hydrolytic activity or used for WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. Individual forms of ATP synthase are indicated: cV M – monomer, cV D – dimer, cV o – oligomer, cV M * and cV D * denote smaller form of the respective complexes.

    Article Snippet: Membranes were blocked in 5% non-fat milk or 3% BSA, dissolved in TBS (Tris-buffered saline containing 150 mM NaCl, 10 mM Tris-HCl, pH 7.5) for 1 h prior to incubations with primary (2 h at room temperature or overnight at 4 °C) antibodies to subunits of ATP synthase (F 1 -α ( ) lot 20D6, F 1 -β (Abcam ab14730), F 1 -γ (GTX 114275), F 1 - δ (GTX101503), F o -a , F o -b (Abcam 117991), F o -c (Abcam 181243), F o -d (GTX 87685), F o -g (GTX 111014), A6L (Biorbyt orb215488), OSCP (Santa Cruz SC-98707), DAPIT (Proteintech 17716-1-AP), MLQ (Proteintech 14704-1-AP), Complex II (SDHA, Abcam 14715), AFG3L2 (Proteintech 14631-1-AP), OPA1 (BD Bio 612606), and actin (Calbiochem CPO1-1EA).

    Techniques: Isolation, Clear Native PAGE, Staining, Activity Assay

    Mitochondria isolated from the respective cell lines were solubilised by digitonin 2 g/g and separated on blue-native PAGE (BNE). WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. ATP synthase forms: cV M – monomer, cV D – dimer, F 1 +c − F 1 and c subunits and F 1 subcomplexes.

    Journal: bioRxiv

    Article Title: MLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthase

    doi: 10.1101/2020.02.03.931709

    Figure Lengend Snippet: Mitochondria isolated from the respective cell lines were solubilised by digitonin 2 g/g and separated on blue-native PAGE (BNE). WB detection of F1-α, Fo-a, A6L, DAPIT and MLQ subunits. ATP synthase forms: cV M – monomer, cV D – dimer, F 1 +c − F 1 and c subunits and F 1 subcomplexes.

    Article Snippet: Membranes were blocked in 5% non-fat milk or 3% BSA, dissolved in TBS (Tris-buffered saline containing 150 mM NaCl, 10 mM Tris-HCl, pH 7.5) for 1 h prior to incubations with primary (2 h at room temperature or overnight at 4 °C) antibodies to subunits of ATP synthase (F 1 -α ( ) lot 20D6, F 1 -β (Abcam ab14730), F 1 -γ (GTX 114275), F 1 - δ (GTX101503), F o -a , F o -b (Abcam 117991), F o -c (Abcam 181243), F o -d (GTX 87685), F o -g (GTX 111014), A6L (Biorbyt orb215488), OSCP (Santa Cruz SC-98707), DAPIT (Proteintech 17716-1-AP), MLQ (Proteintech 14704-1-AP), Complex II (SDHA, Abcam 14715), AFG3L2 (Proteintech 14631-1-AP), OPA1 (BD Bio 612606), and actin (Calbiochem CPO1-1EA).

    Techniques: Isolation, Blue Native PAGE

    (A) MLQ KO and control cells were radioactively labelled for 3h with 35 S-methionin/cysteine and subsequently chased with cold methionine for 1, 2, and 3 days. Cells were harvested, solubilised with triton X-100 and ATP synthase was isolated by immune-affinity purification using ATP synthase immunocapture kit. IP-ATP synthase was than analysed by SDS-PAGE. Quantification of the radioactive signal of all ATP synthase subunits shows uniform kinetics of degradation in control HEK cells (B) , while (C) MLQ KO cells displayed faster turnover of subunits F o -a and A6L (red lines) but stabilization of the F 1 subunits (α and β, green lines) compared to subunits b, d and OSCP of the external stalk (blue line). Similar stabilisation of F 1 subunits show ΔTA cells ( E ) compared to control cybrids ( D ) as well as rho 0 cells ( G ) compared to control rho + cells ( F ).

    Journal: bioRxiv

    Article Title: MLQ is responsible for stabilisation of subunit a in the holoenzyme of mammalian ATP synthase

    doi: 10.1101/2020.02.03.931709

    Figure Lengend Snippet: (A) MLQ KO and control cells were radioactively labelled for 3h with 35 S-methionin/cysteine and subsequently chased with cold methionine for 1, 2, and 3 days. Cells were harvested, solubilised with triton X-100 and ATP synthase was isolated by immune-affinity purification using ATP synthase immunocapture kit. IP-ATP synthase was than analysed by SDS-PAGE. Quantification of the radioactive signal of all ATP synthase subunits shows uniform kinetics of degradation in control HEK cells (B) , while (C) MLQ KO cells displayed faster turnover of subunits F o -a and A6L (red lines) but stabilization of the F 1 subunits (α and β, green lines) compared to subunits b, d and OSCP of the external stalk (blue line). Similar stabilisation of F 1 subunits show ΔTA cells ( E ) compared to control cybrids ( D ) as well as rho 0 cells ( G ) compared to control rho + cells ( F ).

    Article Snippet: Membranes were blocked in 5% non-fat milk or 3% BSA, dissolved in TBS (Tris-buffered saline containing 150 mM NaCl, 10 mM Tris-HCl, pH 7.5) for 1 h prior to incubations with primary (2 h at room temperature or overnight at 4 °C) antibodies to subunits of ATP synthase (F 1 -α ( ) lot 20D6, F 1 -β (Abcam ab14730), F 1 -γ (GTX 114275), F 1 - δ (GTX101503), F o -a , F o -b (Abcam 117991), F o -c (Abcam 181243), F o -d (GTX 87685), F o -g (GTX 111014), A6L (Biorbyt orb215488), OSCP (Santa Cruz SC-98707), DAPIT (Proteintech 17716-1-AP), MLQ (Proteintech 14704-1-AP), Complex II (SDHA, Abcam 14715), AFG3L2 (Proteintech 14631-1-AP), OPA1 (BD Bio 612606), and actin (Calbiochem CPO1-1EA).

    Techniques: Control, Isolation, Affinity Purification, SDS Page